It was found that Concanavalin A (Con A) accelerates the rates of hydrolysis of E. coli beta-galactosidase and yeast invertase by binding to the product (glucose) formed in the reaction. The effect of Con A can be made more significant by adding fresh Con A, as the initially added Con A becomes saturated. In this fashion, 38% of sucrose could be hydrolysed in the presence of Con A, instead of 22% hydrolysis observed without the presence of lectin.